Compact spaces generated by retractions

We study compact spaces which are obtained from metric compacta by iterating the operation of inverse limit of continuous sequences of retractions. We denote this class by R. Allowing continuous images in the definition of class R, one obtains a strictly larger class, which we denote by RC. We show that every space in class RC is either Corson compact or else contains a copy of the ordinal segment $[0,\omega_1]$. This improves a result of Kalenda, where the same was proved for the class of continuous images of Valdivia compacta. We prove that spaces in class R do not contain cutting P-points (see the definition below), which provides a tool for finding spaces in RC minus R. Finally, we study linearly ordered spaces in class RC. We prove that scattered linearly ordered compacta belong to RC and we characterize those ones which belong to R. We show that there are only 5 types (up to order isomorphism) of connected linearly ordered spaces in class R and all of them are Valdivia compact. Finally, we find a universal pre-image for the class of all linearly ordered Valdivia compacta.Comment: Minor corrections; added two statements on linearly ordered compacta. The paper has 21 pages and 2 diagram

A new characterization for the m-quasiinvariants of S_n and explicit basis for two row hook shapes

In 2002, Feigin and Veselov defined the space of m-quasiinvariants for any Coxeter group, building on earlier work of Chalykh and Veselov. While many properties of those spaces were proven from this definition, an explicit computation of a basis was only done in certain cases. In particular, Feigin and Veselov computed bases for the m-quasiinvariants of dihedral groups, including S_3, and Felder and Veselov computed the non-symmetric m-quasiinvariants of lowest degree for general S_n. In this paper, we provide a new characterization of the m-quasiinvariants of S_n, and use this to provide a basis for the isotypic component indexed by the partition [n-1,1]. This builds on a previous paper in which we computed a basis for S_3 via combinatorial methods.Comment: 26 pages, uses youngtab.st

Cyclic AMP Receptor Protein from Yeast Mitochondria

We have identified and characterized a cyclic AMP receptor protein in mitochondria of the yeast Saccharomyces cerevisiae. The binding is specific for cyclic nucleotides, particularly for cyclic AMP which is bound with high affinity (Kd of 10(-9) M) at 1 to 5 pmol/mg of mitochondrial protein. The mitochondrial cyclic AMP receptor is synthesized on cytoplasmic ribosomes and has an apparent molecular weight of 45,000 as determined by photoaffinity labeling. It is localized in the inner mitochondrial membrane and faces the intermembrane space. Cross-contamination of mitochondrial inner membranes by plasma membranes or soluble cytoplasmic proteins is excluded